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Information on EC 3.4.22.57 - caspase-4 and Organism(s) Homo sapiens and UniProt Accession P49662

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.57 caspase-4
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P49662 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/- but also cleaves at Asp-Glu-Val-Asp-/-
Synonyms
caspase-4, caspase 4, casp-4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C14.007
-
-
-
-
Cas4
-
-
CASP-4
-
-
-
-
caspase 4
-
-
-
-
caspase-4
-
-
ICE(rel)-II
-
-
-
-
ICH-2 protease
-
-
-
-
ICH-3 protease
-
-
-
-
ICH3 protease
-
-
-
-
TX
-
-
-
-
TX protease
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
182762-08-9
-
216503-96-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Tyr-Val-Ala-Asp-4-nitroanilide + H2O
acetyl-Tyr-Val-Ala-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
?
Ac-Leu-Glu-Val-Asp-7-amido-4-trifluoro methylcoumarin + H2O
7-amino-4-trifluoromethylcoumarin + Ac-Leu-Glu-Val-Asp
show the reaction diagram
-
10 microM, 2 h, 37°C, reaction stopped with HCl
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-LEVD-4-nitroanilide + H2O
acetyl-LEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-LEVDGW-amide + H2O
?
show the reaction diagram
-
preferred peptide substrate
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
show the reaction diagram
-
WEHD is the optimal tetrapeptide recognition motif
-
-
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YVAD-amido-4-methylcoumarin + H2O
acetyl-YVAD + amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
cowpox serpin CrmA + H2O
?
show the reaction diagram
-
-
-
-
?
LEVD-7-amido-4-trifluoromethylcoumarin + H2O
LEVD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
p35 + H2O
?
show the reaction diagram
-
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
show the reaction diagram
-
-
-
-
?
pro-caspase-3 + H2O
p12 + pro-p17
show the reaction diagram
-
-
-
?
procaspase-1 + H2O
caspase-1 + ?
show the reaction diagram
procaspase-9 + H2O
caspase-9 + ?
show the reaction diagram
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-YVAD-amido-4-methylcoumarin + H2O
succinyl-YVAD + amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
LEVD-7-amido-4-trifluoromethylcoumarin + H2O
LEVD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
procaspase-1 + H2O
caspase-1 + ?
show the reaction diagram
procaspase-9 + H2O
caspase-9 + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-YVD-aldehyde
IC50: 748 nM
iodoacetamide
-
iodoacetic acid
-
acetyl-AEVD-aldehyde
-
-
acetyl-DEVD-aldehyde
-
-
acetyl-IETD-aldehyde
-
-
acetyl-WEHD-aldehyde
-
-
acetyl-YVAD-aldehyde
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
-
cowpox serpin CrmA
-
LEVD-CHO
-
a caspase-4 inhibitor, suppresses both the apoptosis and caspase-9 activation
N-acetyl-LEVD-CHO
-
-
N-tert-butyloxycarbonyl-AEVD-aldehyde
-
-
N-tert-butyloxycarbonyl-IETD-aldehyde
-
-
OspC3
-
the effector molecule of Shigella flexneri interacts with the caspase-4-p19 subunit and inhibits its activation by preventing caspase-4-p19 and caspase-4-p10 heterodimerization by depositing the conserved OspC3 X1-Y-X2-D-X3 motif at the putative catalytic pocket of caspase-4
-
Z-LEVD-fluoromethylketone
-
caspase-4, -5, and -1 inhibitor
Z-VAD
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hepatocyte growth factor
-
-
-
interleukin 6
-
-
Leukemia inhibitory factor
-
-
-
tunicamycin
-
activates caspase-4. Activation of caspase-4 preceeds that of caspase-9
additional information
-
increase of caspase-4 expression by reduced expression of Teashirt3
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.681
acetyl-Tyr-Val-Ala-Asp-4-nitroanilide
pH 7.0, 30°C
0.032
acetyl-DEVD-4-nitroanilide
-
pH 7.5, 30°C
0.35
acetyl-DQMD-4-nitroanilide
-
pH 7.5, 30°C
0.044
acetyl-LEVD-4-nitroanilide
-
pH 7.5, 30°C
0.43
acetyl-LEVDGW-amide
-
pH 7.5, 30°C
0.205
acetyl-VEID-4-nitroanilide
-
pH 7.5, 30°C
0.72
acetyl-VQVD-4-nitroanilide
-
pH 7.5, 30°C
0.031 - 0.079
acetyl-WEHD-7-amido-4-methylcoumarin
0.031
acetyl-YEVD-4-nitroanilide
-
pH 7.5, 30°C
0.874
acetyl-YVAD-4-nitroanilide
-
pH 7.5, 30°C
0.035
acetyl-YVAD-amido-4-methylcoumarin
-
pH 7.5
0.048 - 0.09
succinyl-YVAD-4-nitroanilide
0.09
succinyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
acetyl-WEHD 7-amido-4-methylcoumarin
-
at pH 7.0 and pH 7.5
0.5
acetyl-YVAD-amido-4-methylcoumarin
-
pH 7.5
1.07 - 1.1
succinyl-YVAD-4-nitroanilide
0.4
succinyl-YVAD-amido-4-methylcoumarin
-
pH 7.5, 37°C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000375
acetyl-AEVD-aldehyde
-
pH 7.5, 25°C
0.000132 - 0.00015
acetyl-DEVD-aldehyde
0.0004
acetyl-IETD-aldehyde
-
pH 7.5, 25°C
0.000097
acetyl-WEHD-aldehyde
-
pH 7.5, 25°C
0.00002 - 0.000362
acetyl-YVAD-aldehyde
0.0000011
cowpox serpin CrmA
-
pH 7.5, 25°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000748
acetyl-YVD-aldehyde
Homo sapiens
IC50: 748 nM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
reaction with acetyl-WEHD-7-amido-4-methylcoumarin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
2 h incubation time
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary, activated
Manually annotated by BRENDA team
-
caspase-4 is upregulated in lymphoblastoid cells
Manually annotated by BRENDA team
-
neuroblastoma cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evolution
malfunction
physiological function
additional information
-
elevated caspase activity in Pt1 cells is an outcome of increased caspase-4 activation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP4_HUMAN
377
0
43262
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
x * 35000, active enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 35000, active enzyme, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
synthesized as larger proenzyme which is proteolytically processed to form heterodimeric active enzyme
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
knockdown expression of caspase-4 with siRNA in keratinocytes, overexpression of active caspase-4 rescues UVB-induced secretion of IL-1b by caspase-4 knockdown keratinocytes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
since caspase-4 (C258A) purified from an Escherichia coli host forms aggregates, monomeric proteins including full-length caspase-4, caspase-4 (C258A), and the CARD domain of caspase-4 are purified from the insect cell system
recombinant His6-tagged enzyme
-
recombinant T7-tagged enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
full-length clones are originally transfected into various host cells, including COS-M6, RAT-1 and HeLa
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Mus musculus
-
expression in baculovirus-infected insect cells as 30000 Da proteins lacking the propeptide. Automaturation into p20 and p10 subunits occurs within the cells
-
expression in Escherichia coli
-
expression of wild-type, native caspase-4, of C-terminal Myc-tagged wild-type vcaspase-4, and of caspase-4 mutant C285A in COS-1 cells, co-expression with caspase-1
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
apoptosis-independent cell death is accompanied by increased expression of the inflammatory marker, caspase-4. Caspase-4 is upregulated in Pt1 cells and induced by interferons
-
c-Rel as well as other endoplasmic reticulum stress genes directly modulate expression of caspase-4
-
c-Rel is a negative regulator of caspase-4, e.g. in EBV lymphoblastoid cells
-
caspase-4 protein expression is strongly induced in the lesional stratum corneum of patients suffering from psoriasis, a common chronic inflammatory disease
-
enhancement of nuclear factor-kappaB activity by p65 (RelA) overexpression increases the expression of caspase-4 at both mRNA and protein levels
-
mRNA expression of the pro-form of caspase-4 is up-regulated 2fold after poly-I:C stimulation
-
the dominant negative form of IkappaBalpha suppresses the expression of caspase-4
-
tunicamycin and thapsigargin induce caspase-4 mRNA expression and protein activation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garcia-Calvo, M.; Peterson, E.P.; Leiting, B.; Ruel, R.; Nicholson, D.W.; Thornberry, N.A.
Inhibition of human caspases by peptide-based and macromolecular inhibitors
J. Biol. Chem.
273
32608-32613
1998
Homo sapiens
Manually annotated by BRENDA team
Garcia-Calvo, M.; Peterson, E.P.; Rasper, D.M.; Vaillancourt, J.P.; Zamboni, R.; Nicholson, D.W.; Thornberry, N.A.
Purification and catalytic properties of human caspase family members
Cell Death Differ.
6
362-369
1999
Homo sapiens
Manually annotated by BRENDA team
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens
Manually annotated by BRENDA team
Thornberry, N.A.; Rano, T.A.; Peterson, E.P.; et al.
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
J. Biol. Chem.
272
17907-17911
1997
Homo sapiens
Manually annotated by BRENDA team
Talanian, R.V.; Quinlan, C.; Trautz, S.; Hackett, M.C.; Mankovich, J.A.; Banach, D.; Ghayur, T.; Brady, K.D.; Wong, W.W.
Substrate specificities of caspase family proteases
J. Biol. Chem.
272
9677-9682
1997
Homo sapiens
Manually annotated by BRENDA team
Margolin, N.; Raybuck, S.A.; Wilson, K.P.; Chen, W.; Fox, T.; Gu, Y.; Livingston, D.J.
Substrate and inhibitor specificity of interleukin-1beta-converting enzyme and related caspases
J. Biol. Chem.
272
7223-7228
1997
Homo sapiens
Manually annotated by BRENDA team
Munday N.A.; Vaillancourt J.P.; Ali A.; Casano F.J.; Miller D.K.; Molineaux S.M.; Yamin T.T.; Yu V.L.; Nicholson D.W.
Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases
J. Biol. Chem.
270
15870-15876
1995
Homo sapiens (P49662)
Manually annotated by BRENDA team
Kamada, S.; Funahashi, Y.; Tsujimoto, Y.
Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases
Cell Death Differ.
4
473-478
1997
Homo sapiens
Manually annotated by BRENDA team
Fassy, F.; Krebs, O.; Rey, H.; Komara, B.; Gillard, C.; Capdevila, C.; Yea, C.; Faucheu, C.; Blanchet, A.M.; Miossec, C.; Diu-Hercend, A.
Enzymic activity of two caspases related to interleukin-1beta-converting enzyme
Eur. J. Biochem.
253
76-83
1998
Homo sapiens
Manually annotated by BRENDA team
Faucheu, C.; Diu, A.; Chan, A.W.E.; Blanchet, A.M.; Miossec, C.; Herve, F.; Collard-Dutilleul, V.; Gu, Y.; Aldape, R.A.; Lippke, J.A.; Rocher, C.; Su, M.S.S.; Livingston, D.J.; Hercend, T.; Lalanne, J.L.
A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells
EMBO J.
14
1914-1922
1995
Homo sapiens (P49662)
Manually annotated by BRENDA team
Kamens, J.; Paskind, M.; Hugunin, M.; Talanian, R.V.; Allen, H.; Banach, D.; Bump, N.J.; Hackett, M.C.; Johnston, C.G.; Li, P.; Mankovich, J.A.; Terranova, M.; Ghayur, T.
Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases
J. Biol. Chem.
270
15250-15256
1995
Homo sapiens (P49662)
Manually annotated by BRENDA team
Wang, X.; Narayanan, M.; Bruey, J.M.; Rigamonti, D.; Cattaneo, E.; Reed, J.C.; Friedlander, R.M.
Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell death
Biochim. Biophys. Acta
1762
742-754
2006
Homo sapiens
Manually annotated by BRENDA team
Hitomi, J.; Katayama, T.; Eguchi, Y.; Kudo, T.; Taniguchi, M.; Koyama, Y.; Manabe, T.; Yamagishi, S.; Bando, Y.; Imaizumi, K.; Tsujimoto, Y.; Tohyama, M.
Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
J. Cell Biol.
165
347-356
2004
Homo sapiens
Manually annotated by BRENDA team
Mulugeta, S.; Maguire, J.A.; Newitt, J.L.; Russo, S.J.; Kotorashvili, A.; Beers, M.F.
Misfolded BRICHOS SP-C mutant proteins induce apoptosis via caspase-4- and cytochrome c-related mechanisms
Am. J. Physiol. Lung Cell Mol. Physiol.
293
L720-L729
2007
Homo sapiens
Manually annotated by BRENDA team
Lakshmanan, U.; Porter, A.G.
Caspase-4 interacts with TNF receptor-associated factor 6 and mediates lipopolysaccharide-induced NF-kappaB-dependent production of IL-8 and CC chemokine ligand 4 (macrophage-inflammatory protein-1)
J. Immunol.
179
8480-8490
2007
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team
Yukioka, F.; Matsuzaki, S.; Kawamoto, K.; Koyama, Y.; Hitomi, J.; Katayama, T.; Tohyama, M.
Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis
Neurochem. Int.
52
683-687
2008
Homo sapiens
Manually annotated by BRENDA team
Koehn, S.; Trueck, M.; Poehlmann, T.G.; Schleussner, E.; Markert, U.R.; Seyfarth, L.
Assessment of caspase-4 released free AFC by RP-HPLC and fluorescence detection
J. Chromatogr. B
874
111-114
2008
Homo sapiens
Manually annotated by BRENDA team
Kajiwara, Y.; Akram, A.; Katsel, P.; Haroutunian, V.; Schmeidler, J.; Beecham, G.; Haines, J.L.; Pericak-Vance, M.A.; Buxbaum, J.D.
FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4
PLoS ONE
4
e5071
2009
Homo sapiens, no activity in Mus musculus
Manually annotated by BRENDA team
Sollberger, G.; Strittmatter, G.E.; Kistowska, M.; French, L.E.; Beer, H.D.
Caspase-4 is required for activation of inflammasomes
J. Immunol.
188
1992-2000
2012
Homo sapiens
Manually annotated by BRENDA team
Yamamuro, A.; Kishino, T.; Ohshima, Y.; Yoshioka, Y.; Kimura, T.; Kasai, A.; Maeda, S.
Caspase-4 directly activates caspase-9 in endoplasmic reticulum stress-induced apoptosis in SH-SY5Y cells
J. Pharmacol. Sci.
115
239-243
2011
Homo sapiens
Manually annotated by BRENDA team
Valentin-Acevedo, A.; Sinquett, F.L.; Covey, L.R.
c-Rel deficiency increases caspase-4 expression and leads to ER stress and necrosis in EBV-transformed cells
PLoS ONE
6
e25467
2011
Homo sapiens
Manually annotated by BRENDA team
Kobayashi, T.; Ogawa, M.; Sanada, T.; Mimuro, H.; Kim, M.; Ashida, H.; Akakura, R.; Yoshida, M.; Kawalec, M.; Reichhart, J.M.; Mizushima, T.; Sasakawa, C.
The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection
Cell Host Microbe
13
570-583
2013
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Grimstad, O.; Husebye, H.; Espevik, T.
TLR3 mediates release of IL-1beta and cell death in keratinocytes in a caspase-4 dependent manner
J. Dermatol. Sci.
72
45-53
2013
Homo sapiens
Manually annotated by BRENDA team
Kajiwara, Y.; Schiff, T.; Voloudakis, G.; Gama Sosa, M.A.; Elder, G.; Bozdagi, O.; Buxbaum, J.D.
A critical role for human caspase-4 in endotoxin sensitivity
J. Immunol.
193
335-343
2014
Homo sapiens
Manually annotated by BRENDA team
Yang, H.J.; Wang, M.; Wang, L.; Cheng, B.F.; Lin, X.Y.; Feng, Z.W.
NF-kappaB regulates caspase-4 expression and sensitizes neuroblastoma cells to Fas-induced apoptosis
PLoS ONE
10
e0117953
2015
Homo sapiens
Manually annotated by BRENDA team
Schmid-Burgk, J.L.; Gaidt, M.M.; Schmidt, T.; Ebert, T.S.; Bartok, E.; Hornung, V.
Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome in human myeloid cells
Eur. J. Immunol.
45
2911-2917
2015
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team
Vigano, E.; Diamond, C.E.; Spreafico, R.; Balachander, A.; Sobota, R.M.; Mortellaro, A.
Human caspase-4 and caspase-5 regulate the one-step non-canonical inflammasome activation in monocytes
Nat. Commun.
6
8761
2015
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team
Lagrange, B.; Benaoudia, S.; Wallet, P.; Magnotti, F.; Provost, A.; Michal, F.; Martin, A.; Di Lorenzo, F.; Py, B.F.; Molinaro, A.; Henry, T.
Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11
Nat. Commun.
9
242
2018
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team
Casson, C.N.; Yu, J.; Reyes, V.M.; Taschuk, F.O.; Yadav, A.; Copenhaver, A.M.; Nguyen, H.T.; Collman, R.G.; Shin, S.
Human caspase-4 mediates noncanonical inflammasome activation against gram-negative bacterial pathogens
Proc. Natl. Acad. Sci. USA
112
6688-6693
2015
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team
An, J.; Kim, S.H.; Hwang, D.; Lee, K.E.; Kim, M.J.; Yang, E.G.; Kim, S.Y.; Chung, H.S.
Caspase-4 disaggregates lipopolysaccharide micelles via LPS-CARD interaction
Sci. Rep.
9
826
2019
Homo sapiens (P49662), Homo sapiens
Manually annotated by BRENDA team